Phosphorylation of the MAP kinase ERK2 promotes its homodimerization and nuclear translocation

Article Abstract:

The phosphorylation of the membrane-associated protein (MAP) kinase ERK2 promotes the formation of homodimers consisting of two phosphorylated ERK2 or one phosphorylated and one native ERK2. This dimerization process is an important process before ERK2 is translocated to the nucleus. Once in the nucleus, ERK2 phosphorylates nuclear targets to complete the signal transduction pathway. Other MAP kinases exhibit a similar tendency to form dimers indicating that dimerization may be a component of the mechanism of action of these enzymes.

Research, Physiological aspects, Cellular signal transduction, Protein kinases

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Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

Article Abstract:

Phosphorylation on a threonine and a tyrosine residue within the phosphorylation lip has solved the structure of the active form of ERK2, the MAP kinase. The refolded lip aligns the phosphothreonine and phosphotyrosine. The lip and neighboring structures showed conformational changes, particularly the P+1 site, the C-terminal extension and helix and the MAP kinase insertion.

Observations, Protein tyrosine kinase, Protein-tyrosine kinase, Phosphorylation, Threonine

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